Human islet amyloid polypeptide: A therapeutic target for the management of type 2 diabetes mellitus. [PDF]
Roham PH, Save SN, Sharma S.
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Polyphenol Effect on the Interactions Between Functional Proteins and Amyloid Fibrils
Among a wide variety of protein-protein interactions, the complexation of functionally important proteins with pathogenic protein aggregates (amyloid fibrils) attracts particular interest in view of its possible contribution to amyloid cytotoxicity.
U. Malovytsia +5 more
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Exploring the Role of Anionic Lipid Nanodomains in the Membrane Disruption and Protein Folding of Human Islet Amyloid Polypeptide Oligomers on Lipid Membrane Surfaces Using Multiscale Molecular Dynamics Simulations. [PDF]
Nguyen N +4 more
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Human Islet Amyloid Polypeptide Overexpression in INS-1E Cells Influences Amylin Oligomerization under ER Stress and Oxidative Stress. [PDF]
Yoo YM, Joo SS.
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Human islet amyloid polypeptide (hIAPP) oligomers, formed through an accumulation pathway, are toxic to insulin-secreting pancreatic β-cells and are considered to contribute for β-cell death and insulin deficiency commonly observed in type 2 diabetes ...
Mahboobeh Nazari +7 more
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FoxA2 and RNA Pol II mediate human islet amyloid polypeptide turnover in ER-stressed pancreatic β-cells. [PDF]
Chatterjee Bhowmick D +3 more
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Regulation of divalent metal ions to the aggregation and membrane damage of human islet amyloid polypeptide oligomers. [PDF]
Wang Y, Meng F, Lu T, Wang C, Li F.
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Structural and morphological dynamics of "on-path" and "off-path" oligomers of human islet amyloid polypeptide. [PDF]
Warren D, Sitton J, Kurouski D.
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